BMRB Entry 18309

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18309

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Title:
Chemical Shift 1H, 13C, 15N Assignments of N-terminal domain of Thermotoga Maritima flagellar motor protein FliG
Deposition date:
2012-03-01
Original release date:
2012-06-13
Authors:
Levenson, Robert
Citation:

Citation: Levenson, Robert; Zhou, Hongjun; Dahlquist, Frederick. "Structural insights into the interaction between the bacterial flagellar motor proteins FliF and FliG."  Biochemistry 51, 5052-5060 (2012).
PubMed: 22670715

Assembly members:

Assembly members:
FliGn, polymer, 122 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Thermotoga maritima   Taxonomy ID: 2336   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Thermotoga maritima

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pJY5

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FliGn: MDHHHHHHHHASENLYFQGH MPEKKIDGRRKAAVLLVALG PEKAAQVMKHLDEETVEQLV VEIANIGRVTPEEKKQVLEE FLSLAKAKEMISEGGIEYAK KVLEKAFGPERARKIIERLT SS

Data sets:
Data typeCount
13C chemical shifts191
15N chemical shifts91
1H chemical shifts91

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1FliGn, chain 11
2FliGn, chain 21

Entities:

Entity 1, FliGn, chain 1 122 residues - Formula weight is not available

1   METASPHISHISHISHISHISHISHISHIS
2   ALASERGLUASNLEUTYRPHEGLNGLYHIS
3   METPROGLULYSLYSILEASPGLYARGARG
4   LYSALAALAVALLEULEUVALALALEUGLY
5   PROGLULYSALAALAGLNVALMETLYSHIS
6   LEUASPGLUGLUTHRVALGLUGLNLEUVAL
7   VALGLUILEALAASNILEGLYARGVALTHR
8   PROGLUGLULYSLYSGLNVALLEUGLUGLU
9   PHELEUSERLEUALALYSALALYSGLUMET
10   ILESERGLUGLYGLYILEGLUTYRALALYS
11   LYSVALLEUGLULYSALAPHEGLYPROGLU
12   ARGALAARGLYSILEILEGLUARGLEUTHR
13   SERSER

Samples:

sample_1: FliGn, [U-100% 13C; U-100% 15N], 400 ± 100 uM; Sodium Phosphate 50 mM; NaCl 100 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 125 mM; pH: 6.5; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

ANSIG, Kraulis - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

BMRB 18310
GB AAD35312 ABQ46724 ACB09081 ADA66942 AGL49144
REF NP_228035 WP_004082903 WP_008193872 WP_011943308 WP_012310706
SP Q9WY63
AlphaFold Q9WY63

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks